Blomenröhr M, Kühne R, Hund E, Leurs R, Bogerd J, ter Laak T
Department of Experimental Zoology, Utrecht University, The Netherlands.
FEBS Lett. 2001 Jul 20;501(2-3):131-4. doi: 10.1016/s0014-5793(01)02647-3.
The negatively charged side chain of an Asp residue in transmembrane domain 2 is likely to play an important role in receptor signalling since it is highly conserved in the whole family of G protein-coupled receptors, except in mammalian gonadotropin-releasing hormone (GnRH) receptors. In this paper we show that the conserved Asp(90) of the catfish GnRH receptor can be substituted by a neutral Asn(90) without abolishing receptor signalling if another negatively charged Glu(93) is introduced in a proximal region of the receptor interior, thereby mimicking the Glu(90)-Lys(121) salt bridge of mammalian GnRH receptors.
